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Open data
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Basic information
Entry | Database: PDB / ID: 2btp | ||||||
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Title | 14-3-3 Protein Theta (Human) Complexed to Peptide | ||||||
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![]() | SIGNALING PROTEIN/PEPTIDE / 14-3-3 / PHOSPHOSERINE / STRUCTURAL GENOMICS CONSORTIUM / PHOSPHORYLATION / COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE) / SIGNALING PROTEIN-PEPTIDE complex | ||||||
Function / homology | ![]() negative regulation of monoatomic ion transmembrane transport / small GTPase-mediated signal transduction / Regulation of localization of FOXO transcription factors / Activation of BAD and translocation to mitochondria / protein targeting / SARS-CoV-2 targets host intracellular signalling and regulatory pathways / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / RHO GTPases activate PKNs / 14-3-3 protein binding ...negative regulation of monoatomic ion transmembrane transport / small GTPase-mediated signal transduction / Regulation of localization of FOXO transcription factors / Activation of BAD and translocation to mitochondria / protein targeting / SARS-CoV-2 targets host intracellular signalling and regulatory pathways / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / RHO GTPases activate PKNs / 14-3-3 protein binding / substantia nigra development / Translocation of SLC2A4 (GLUT4) to the plasma membrane / TP53 Regulates Metabolic Genes / transmembrane transporter binding / protein domain specific binding / focal adhesion / negative regulation of DNA-templated transcription / synapse / signal transduction / protein-containing complex / extracellular exosome / identical protein binding / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Elkins, J.M. / Johansson, A.C.E. / Smee, C. / Yang, X. / Sundstrom, M. / Edwards, A. / Arrowsmith, C. / Doyle, D.A. / Structural Genomics Consortium (SGC) | ||||||
![]() | ![]() Title: Structural Basis for Protein-Protein Interactions in the 14-3-3 Protein Family. Authors: Yang, X. / Lee, W.H. / Sobott, F. / Papagrigoriou, E. / Robinson, C.V. / Grossmann, J.G. / Sundstrom, M. / Doyle, D.A. / Elkins, J.M. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 103.5 KB | Display | ![]() |
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PDB format | ![]() | 78.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 453.1 KB | Display | ![]() |
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Full document | ![]() | 455.8 KB | Display | |
Data in XML | ![]() | 17.4 KB | Display | |
Data in CIF | ![]() | 23.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2bq0C ![]() 2br9C ![]() 2c23C ![]() 2c63C ![]() 2c74C ![]() 1qjaS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS ensembles :
NCS oper: (Code: given Matrix: (-0.98666, -0.16262, -0.00741), Vector: Details | THE ENTRY IS MARKED TETRAMERIC SINCE THE CHAINS AAND B ARE BOUND TO PEPTIDES P AND Q. THE PROTEINITSELF IS DIMERIC IN NATURE. | |
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Components
#1: Protein | Mass: 29234.906 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: THE MAMMALIAN GENE COLLECTION, I.M.A.G.E. CONSORTIUM CLONEID 6164592 Plasmid: PNIC-BSA4 / Production host: ![]() ![]() #2: Protein/peptide | Mass: 795.781 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: PHOSPHOSERINE AT RESIDUES P 5 AND Q 5 / Source: (synth.) ![]() Compound details | FUNCTION: STRONGLY ACTIVATES PROTEIN KINASE C | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54 % |
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Crystal grow | pH: 8.5 Details: 0.2M SODIUM ACETATE TRIHYDRATE, 0.1M TRISHCL PH8.5,30% PEG4000, pH 8.50 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU-MSC R-AXIS HTC / Detector: IMAGE PLATE / Date: May 21, 2005 / Details: OSMIC MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→34.88 Å / Num. obs: 14743 / % possible obs: 96.4 % / Observed criterion σ(I): 0 / Redundancy: 6.3 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 17.7 |
Reflection shell | Resolution: 2.8→2.95 Å / Redundancy: 5.8 % / Rmerge(I) obs: 0.41 / Mean I/σ(I) obs: 3.5 / % possible all: 93.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1QJA Resolution: 2.8→59.66 Å / Cor.coef. Fo:Fc: 0.942 / Cor.coef. Fo:Fc free: 0.905 / SU B: 29.994 / SU ML: 0.266 / Cross valid method: THROUGHOUT / ESU R Free: 0.395 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 51.8 Å2
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Refinement step | Cycle: LAST / Resolution: 2.8→59.66 Å
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Refine LS restraints |
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